P00909 (TRPC_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tryptophan biosynthesis protein TrpCF

Including the following 2 domains:

1. Indole-3-glycerol phosphate synthase
   Short name=IGPS
   EC=4.1.1.48
2. N-(5'-phospho-ribosyl)anthranilate isomerase
   Short name=PRAI
   EC=5.3.1.24

Gene names

Name:	trpC
Ordered Locus Names:	b1262, JW1254

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	452 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Bifunctional enzyme that catalyzes two sequential steps of tryptophan biosynthetic pathway. The first reaction is catalyzed by the isomerase, coded by the TrpF domain; the second reaction is catalyzed by the synthase, coded by the TrpC domain. HAMAP MF_00134_B
Catalytic activity	N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. HAMAP MF_00134_B 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO2 + H2O. HAMAP MF_00134_B
Pathway	Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5. HAMAP MF_00134_B Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
Subunit structure	Monomer.
Sequence similarities	In the N-terminal section; belongs to the TrpC family. In the C-terminal section; belongs to the TrpF family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis Tryptophan biosynthesis
Molecular function	Decarboxylase Isomerase Lyase
Technical term	3D-structure Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological process	tryptophan biosynthetic process Inferred from direct assay. Source: EcoCyc
Molecular function	indole-3-glycerol-phosphate synthase activity Inferred from direct assay. Source: EcoCyc phosphoribosylanthranilate isomerase activity Inferred from direct assay. Source: EcoCyc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 452

452

Tryptophan biosynthesis protein TrpCF HAMAP MF_00134_B

PRO_0000154277

Regions

Region

1 – 256

256

Indole-3-glycerol phosphate synthase HAMAP MF_00134_B

Region

257 – 452

196

N-(5'-phosphoribosyl)anthranilate isomerase HAMAP MF_00134_B

Experimental info

Sequence conflict

30

1

Missing in CAA23673. Ref.3

Sequence conflict

94

1

Q → R in CAA23664. Ref.1

Sequence conflict

94

1

Q → R in AAA57299. Ref.1

Sequence conflict

94

1

Q → R in CAA23673. Ref.3

Sequence conflict

284

1

Missing in CAA23673. Ref.3

Sequence conflict

293

1

V → D in CAA23673. Ref.3

Sequence conflict

329

1

A → V in CAA23664. Ref.1

Sequence conflict

329

1

A → V in AAA57299. Ref.1

Sequence conflict

329

1

A → V in CAA23673. Ref.3

Sequence conflict

398

1

S → T in CAA23664. Ref.1

Sequence conflict

398

1

S → T in AAA57299. Ref.1

Sequence conflict

398

1

S → T in CAA23673. Ref.3

Sequence conflict

398

1

S → T in AAB60033. Ref.4

Secondary structure

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452

Helix Strand Turn

Details...

Helix

4 – 20

17

Helix

25 – 27

3

Helix

29 – 31

3

Helix

39 – 42

4

Beta strand

45 – 47

3

Beta strand

49 – 54

6

Beta strand

56 – 58

3

Turn

59 – 61

3

Helix

70 – 77

8

Turn

78 – 80

3

Beta strand

82 – 87

6

Helix

90 – 93

4

Helix

99 – 106

8

Beta strand

111 – 115

5

Helix

120 – 128

9

Beta strand

133 – 137

5

Turn

138 – 140

3

Helix

143 – 153

11

Turn

154 – 157

4

Beta strand

159 – 164

6

Helix

167 – 175

9

Beta strand

179 – 184

6

Turn

188 – 191

4

Helix

196 – 201

6

Helix

203 – 205

3

Beta strand

207 – 215

9

Helix

220 – 226

7

Turn

227 – 229

3

Beta strand

231 – 235

5

Helix

237 – 240

4

Helix

245 – 252

8

Helix

265 – 274

10

Beta strand

277 – 282

6

Helix

293 – 302

10

Beta strand

306 – 313

8

Helix

316 – 326

11

Beta strand

329 – 333

5

Helix

339 – 348

10

Beta strand

353 – 360

8

Beta strand

362 – 364

3

Beta strand

375 – 380

6

Helix

391 – 394

4

Beta strand

402 – 407

6

Turn

410 – 412

3

Helix

413 – 417

5

Beta strand

422 – 426

5

Helix

428 – 430

3

Beta strand

431 – 433

3

Helix

439 – 450

12

Sequences

	Sequence		Length	Mass (Da)
	P00909 [UniParc]. Last modified August 29, 2003. Version 3. Checksum: AEAE60B25E61E8A8	FASTA	452	49,361
	10 20 30 40 50 60 MQTVLAKIVA DKAIWVEARK QQQPLASFQN EVQPSTRHFY DALQGARTAF ILECKKASPS 70 80 90 100 110 120 KGVIRDDFDP ARIAAIYKHY ASAISVLTDE KYFQGSFNFL PIVSQIAPQP ILCKDFIIDP 130 140 150 160 170 180 YQIYLARYYQ ADACLLMLSV LDDDQYRQLA AVAHSLEMGV LTEVSNEEEQ ERAIALGAKV 190 200 210 220 230 240 VGINNRDLRD LSIDLNRTRE LAPKLGHNVT VISESGINTY AQVRELSHFA NGFLIGSALM 250 260 270 280 290 300 AHDDLHAAVR RVLLGENKVC GLTRGQDAKA AYDAGAIYGG LIFVATSPRC VNVEQAQEVM 310 320 330 340 350 360 AAAPLQYVGV FRNHDIADVV DKAKVLSLAA VQLHGNEEQL YIDTLREALP AHVAIWKALS 370 380 390 400 410 420 VGETLPAREF QHVDKYVLDN GQGGSGQRFD WSLLNGQSLG NVLLAGGLGA DNCVEAAQTG 430 440 450 CAGLDFNSAV ESQPGIKDAR LLASVFQTLR AY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Gene structure in the tryptophan operon of Escherichia coli. Nucleotide sequence of trpC and the flanking intercistronic regions." Christie G.E., Platt T. J. Mol. Biol. 142:519-530(1980) [PubMed: 7007653] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Nucleotide sequence of the trpD and trpC genes of Salmonella typhimurium." Horowitz H., van Arsdell J., Platt T. J. Mol. Biol. 169:775-797(1983) [PubMed: 6355484] [Abstract] Cited for: SEQUENCE REVISION TO 94 AND 398.
[3]	"The complete nucleotide sequence of the tryptophan operon of Escherichia coli." Yanofsky C., Platt T., Crawford I.P., Nichols B.P., Christie G.E., Horowitz H., van Cleemput M., Wu A.M. Nucleic Acids Res. 9:6647-6668(1981) [PubMed: 7038627] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Molecular evolution of the Escherichia coli chromosome. IV. Sequence comparisons." Milkman R., Bridges M.M. Genetics 133:455-468(1993) [PubMed: 8095913] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:363-377(1996) [PubMed: 9097039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[7]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[8]	"Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: indoleglycerolphosphate synthase from Escherichia coli refined at 2.0-A resolution." Wilmanns M., Priestle J.P., Niermann T., Jansonius J.N. J. Mol. Biol. 223:477-507(1992) [PubMed: 1738159] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), SEQUENCE REVISION TO 319.
[9]	"Crystallization and structure solution at 4-A resolution of the recombinant synthase domain of N-(5'-phosphoribosyl)anthranilate isomerase:indole-3-glycerol-phosphate synthase from Escherichia coli complexed to a substrate analogue." Wilmanns M., Schlagenhauf E., Fol B., Jansonius J.N. Protein Eng. 3:173-180(1990) [PubMed: 2184433] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 257-452.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

V00366 Genomic DNA. Translation: CAA23664.1.
V00372 Genomic DNA. Translation: CAA23673.1.
J01714 Genomic DNA. Translation: AAA57299.1.
U23489 Genomic DNA. Translation: AAB60033.1.
U00096 Genomic DNA. Translation: AAC74344.2.
AP009048 Genomic DNA. Translation: BAA14794.1.

PIR

GWEC. A64874.

RefSeq

NP_415778.2. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JCM	X-ray	2.10	P	1-259	[»]
1PII	X-ray	2.00	A	1-452	[»]
2KZH	NMR	-	A	255-384	[»]

ProteinModelPortal

P00909.

SMR

P00909. Positions 1-452.

ModBase

Search...

Protein-protein interaction databases

IntAct

P00909. 2 interactions.

2D gel databases

ECO2DBASE

F045.4. 6TH EDITION.
F045.5. 6TH EDITION.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000001872; EBESCP00000001872; EBESCG00000001539.
EBESCT00000001873; EBESCP00000001873; EBESCG00000001539.
EBESCT00000015020; EBESCP00000014311; EBESCG00000014080.

GeneID

945519.

GenomeReviews

Gene locus JW1254 in contig AP009048_GR.
Gene locus b1262 in contig U00096_GR.

KEGG

ecj:JW1254.
eco:b1262.

PATRIC

32117784. VBIEscCol129921_1312.

Organism-specific databases

EchoBASE

EB1019.

EcoGene

EG11026. trpC.

Phylogenomic databases

eggNOG

COG0134.

GeneTree

EBGT00050000011501.

HOGENOM

HBG296890.

OMA

YILECKK.

PhylomeDB

P00909.

ProtClustDB

PRK09427.

Enzyme and pathway databases

BioCyc

EcoCyc:PRAI-IGPS.
MetaCyc:PRAI-IGPS.

Gene expression databases

Genevestigator

P00909.

Family and domain databases

HAMAP

MF_00134_B. IGPS_B. Fused.
[Tree]
MF_00135. PRAI. Fused.
[Tree]

InterPro

IPR013785. Aldolase_TIM.
IPR013798. Indole-3-glycerol_P_synth.
IPR001468. Indole-3-GlycerolPSynthase_CS.
IPR001240. PRAI.
IPR011060. RibuloseP-bd_barrel.
[Graphical view]

Gene3D

G3DSA:3.20.20.70. Aldolase_TIM. 2 hits.

KO

K13498.

Pfam

PF00218. IGPS. 1 hit.
PF00697. PRAI. 1 hit.
[Graphical view]

SUPFAM

SSF51366. RibP_bind_barrel. 2 hits.

PROSITE

PS00614. IGPS. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

TRPC_ECOLI

Accession

Primary (citable) accession number: P00909
Secondary accession number(s): P78059, P78234, P94704

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	August 29, 2003
Last modified:	January 25, 2012
This is version 121 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program